Lin A, McNally J, Wool I G
J Biol Chem. 1984 Jan 10;259(1):487-90.
The covalent structure of the rat liver 60 S ribosomal subunit protein L39 was determined. Fourteen tryptic peptides were purified, and the sequence of each was established by a micromanual procedure; they accounted for all 50 residues of L39. The sequence of the NH2-terminal 32 residues of L39, obtained by automated Edman degradation of the intact protein, provided the alignment of the first seven tryptic peptides. Two peptides, CNI (28 residues) and CNII (22 residues), were produced by cleavage of protein L39 with cyanogen bromide and the sequence of CNII was determined by automated Edman degradation. This sequence established the order of tryptic peptides T8 through T14. The carboxyl-terminal amino acids were identified after carboxypeptidase A treatment. Protein L39 contains 50 amino acids and has a molecular weight of 7308. There are indications that a portion of rat L39 is related to a fragment of Escherichia coli ribosomal protein S1.
确定了大鼠肝脏60S核糖体亚基蛋白L39的共价结构。纯化了14个胰蛋白酶肽段，每个肽段的序列通过微手动操作确定；它们涵盖了L39的所有50个残基。通过对完整蛋白进行自动Edman降解获得的L39氨基末端32个残基的序列，确定了前七个胰蛋白酶肽段的排列顺序。用溴化氰裂解蛋白L39产生了两个肽段，CNI（28个残基）和CNII（22个残基），并通过自动Edman降解确定了CNII的序列。该序列确定了胰蛋白酶肽段T8至T14的顺序。经羧肽酶A处理后鉴定出羧基末端氨基酸。蛋白L39含有50个氨基酸，分子量为7308。有迹象表明大鼠L39的一部分与大肠杆菌核糖体蛋白S1的一个片段相关。
